@article{10.37349/ei.2026.1003234,
abstract = {Vaccines can be highly safe and effective tools for disease prevention. However, improvements in the areas of cost, ease of manufacture, distribution, and administration are sought in the next generation of vaccine platforms. A promising candidate is the recombinant flagellin fusion protein platform, which comprises a protein antigen of interest genetically fused to the bacterial protein flagellin. As flagellin stimulates two distinct pattern recognition receptors of the human innate immune system (Toll-like receptor 5 and nucleotide-binding and oligomerization domain-like receptor family apoptosis inhibitory protein) and contains helper T-cell epitopes, it is capable of serving as both a carrier and an adjuvant for the target antigen. Studies in animal models and human clinical trials have shown that flagellin fusion proteins can induce diverse humoral (including various subtypes of IgG), mucosal (including secreted IgA), and cell-mediated (TH1 and TH2 CD4+ helper T-cell and CD8+ cytotoxic T-cell) responses to the covalently linked antigen. Such fusions are also capable of eliciting protective immunity in diverse experimental models of infection and cancer. They are effective via numerous routes of administration, including intranasal delivery, without the requirement for adjuvant or complex delivery vehicles. This review aims to cover recent progress in the investigation of flagellin fusion proteins for their potential to stimulate humoral and cellular immune responses to partner antigens, and their prospects for the prevention or treatment of viral infections and cancer.},
author = {Erridge, Clett},
doi = {10.37349/ei.2026.1003234},
journal = {Exploration of Immunology},
elocation-id = {1003234},
title = {Flagellin fusion proteins as self-adjuvanting vaccines for viral infections and cancer},
url = {https://www.explorationpub.com/Journals/ei/Article/1003234},
volume = {6},
year = {2026}
}